A4021
Nε-Acetyl-L-lysine
Nε-Acetyl-L-lysine
≥98% (TLC)
Sinonimo/i:
N6-acetyl-L-lysine
Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
Scegli un formato
1 G
CHF 116.00
5 G
CHF 376.00
Scegli un formato
Cambia visualizzazione
1 G
CHF 116.00
5 G
CHF 376.00
About This Item
Formula condensata:
CH3CONH(CH2)4CH(NH2)CO2H
Numero CAS:
Peso molecolare:
188.22
Numero CE:
Numero MDL:
Codice UNSPSC:
12352209
ID PubChem:
NACRES:
NA.26
Prodotti consigliati
Nome del prodotto
Nε-Acetyl-L-lysine,
Saggio
≥98% (TLC)
Stato
powder
Concentrazione
50 mg/mL in 80% acetic acid
Colore
colorless to white
Punto di fusione
250 °C (dec.) (lit.)
Temperatura di conservazione
−20°C
Stringa SMILE
CC(=O)NCCCC[C@H](N)C(O)=O
InChI
1S/C8H16N2O3/c1-6(11)10-5-3-2-4-7(9)8(12)13/h7H,2-5,9H2,1H3,(H,10,11)(H,12,13)/t7-/m0/s1
DTERQYGMUDWYAZ-ZETCQYMHSA-N
Cerchi prodotti simili? Visita Guida al confronto tra prodotti
Applicazioni
- Nε-Acetyl L-α Lysine Improves Activity and Stability of α-Amylase at Acidic Conditions: A Comparative Study with other Osmolytes. This study highlights the use of Nε-Acetyl-ʟ-lysine in enhancing the functional stability and activity of α-amylase under acidic conditions, demonstrating its potential as a valuable additive in industrial enzyme applications (Joghee et al., 2020).
Azioni biochim/fisiol
Nε-Acetyl-L-lysine (L-AcK) is an R-chain N-acetylated α amino acid used together with other lysine analogues to differentiate and characterized various aminoacylases and regulator 2 (Sir2) enzymes/sirtuins.
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Scegli una delle versioni più recenti:
Possiedi già questo prodotto?
I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
I clienti hanno visto anche
A Pähler et al.
Chemical research in toxicology, 11(9), 995-1004 (1998-10-07)
Antibodies directed against chemical specific protein modifications are valuable tools to detect and comparatively quantify protein modifications. Both Nepsilon-(dichloroacetyl)-L-lysine and Nepsilon-(trichloroacety)l-L-lysine have been detected as modified amino acids in liver and kidneys of rats treated with perchloroethene (PER) after proteolysis.
T Henle et al.
Zeitschrift fur Lebensmittel-Untersuchung und -Forschung, 198(1), 66-67 (1994-01-01)
After heating N alpha-acetyllysine and glucose for 4 h at 90 degrees C in the dry state and subsequent acid hydrolysis with 7.8 N HCl, preparative fractionation of the dihydrochlorides of furosine and pyridosine was achieved by cation-exchange chromatography. The
Heinz Neumann et al.
Nature chemical biology, 4(4), 232-234 (2008-02-19)
N(epsilon)-acetylation of lysine (1) is a reversible post-translational modification with a regulatory role that rivals that of phosphorylation in eukaryotes. No general methods exist to synthesize proteins containing N(epsilon)-acetyllysine (2) at defined sites. Here we demonstrate the site-specific incorporation of
Ying Huang et al.
Molecular bioSystems, 6(4), 683-686 (2010-03-20)
By overexpressing the C-terminal domain of the ribosomal protein L11 to decrease release factor 1-mediated termination of protein translation, enhanced amber suppression is achieved in E. coli. This enhanced amber suppression efficiency allows the genetic incorporation of three N(epsilon)-acetyl-l-lysines into
Morten B Trelle et al.
Analytical chemistry, 80(9), 3422-3430 (2008-03-15)
Tandem mass spectrometry (MS/MS) is a powerful tool for characterization of post-translationally modified proteins, including epsilon-N-acetyllysine-containing species. Previous reports indicate that epsilon-N-acetyllysine immonium ions are useful marker ions for peptides containing epsilon-N-acetyllysine, but the specificity and sensitivity of these ions
Active Filters
Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..
Contatta l'Assistenza Tecnica.
